Evidence map›Paper›PMID 39571956›Full record

ReviewArchives of biochemistry and biophysics2025

Selenoprotein K at the intersection of cellular pathways.

Atinuke Odunsi, Mariia A Kapitonova, George Woodward, Erfan Rahmani, Farid Ghelichkhani, Jun Liu, Sharon Rozovsky

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Archives of biochemistry and biophysics, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Atinuke OdunsiDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE, USA.
Mariia A KapitonovaDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE, USA.
George WoodwardDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE, USA.
Erfan RahmaniDepartment of Biomedical Engineering, University of Delaware, Newark, DE, USA.
Farid GhelichkhaniDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE, USA.
Jun LiuAsieris Pharmaceuticals, Palo Alto, CA, USA.
Sharon RozovskyDepartment of Chemistry and Biochemistry, University of Delaware, Newark, DE, USA. Electronic address: rozovsky@udel.edu.

Funding

Chemistry-Biology Interface Predoctoral Training Grant 2024-2029T32GM133395 · NIGMS · UNIVERSITY OF DELAWARE · PI Catherine Leimkuhler Grimes · 2019 to 2026
$3.7M
Signaling, Sensing, and Enzymatic Roles of Disordered SelenoproteinsR35GM153494 · NIGMS · UNIVERSITY OF DELAWARE · PI Sharon Rozovsky · 2024 to 2026
$1.1M
Selenoproteins in the ER-associated protein degradation pathwayR01GM121607 · NIGMS · UNIVERSITY OF DELAWARE · PI ROZOVSKY, SHARON · 2017 to 2021
$1.1M
NIGMS NIH HHS R01 GM121607NIGMS NIH HHS R35 GM153494NIGMS NIH HHS T32 GM133395
6 · The paper itself

Abstract

Selenoprotein K (selenok) is linked to the integrated stress response, which helps cells combat stressors and regain normal function. The selenoprotein contains numerous protein interaction hubs and post-translational modification sites and is involved in protein palmitoylation, vesicle trafficking, and the resolution of ER stress. Anchored to the endoplasmic reticulum (ER) membrane, selenok interacts with protein partners to influence their stability, localization, and trafficking, impacting various cellular functions such as calcium homeostasis, cellular migration, phagocytosis, gene expression, and immune response. Consequently, selenok expression level is linked to cancer and neurodegenerative diseases. Because it contains the reactive amino acid selenocysteine, selenok is likely to function as an enzyme. However, highly unusual for enzymes, the protein segment containing the selenocysteine lacks a stable secondary or tertiary structure, yet it includes multiple interaction sites for protein partners and post-translational modifications. Currently, the reason(s) for the presence of the rare selenocysteine in selenok is not known. Furthermore, of selenok's numerous interaction sites, only some have been sufficiently characterized, leaving many of selenok's potential protein partners to be discovered. In this review, we explore selenok's role in various cellular pathways and its impact on human health, thereby highlighting the links between its diverse cellular functions.

Indexed as

SelenoproteinsAnimalsEndoplasmic ReticulumEndoplasmic Reticulum StressHumansNeoplasmsProtein Processing, Post-TranslationalSelenocysteineSelenocysteineselenoprotein K, humanSelenoproteins

Identifiers

PMID39571956
PMCPMC11750610

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.